Please use this identifier to cite or link to this item: https://ahro.austin.org.au/austinjspui/handle/1/11240
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dc.contributor.authorKelly, J Men
dc.contributor.authorTrinder, Den
dc.contributor.authorPhillips, P Aen
dc.contributor.authorCasley, David Jen
dc.contributor.authorKemp, Bruce Een
dc.contributor.authorMooser, Ven
dc.contributor.authorJohnston, Colin Ien
dc.date.accessioned2015-05-16T00:49:44Z
dc.date.available2015-05-16T00:49:44Z
dc.date.issued1990-07-08en
dc.identifier.citationPeptides; 11(4): 857-62en
dc.identifier.govdoc2146598en
dc.identifier.otherPUBMEDen
dc.identifier.urihttps://ahro.austin.org.au/austinjspui/handle/1/11240en
dc.description.abstractThe molecular recognition hypothesis, that peptide ligands and their receptor binding sites are encoded by complementary nucleotide sequences, was tested for arginine vasopressin (AVP) and its V1 receptor. Binding of [125I] [d(CH2)5,Sar7]AVP (a selective V1 vasopressin antagonist radioligand) or [3H]AVP to rat liver plasma membranes was inhibited by peptides known to bind to V1 receptors but not by the AVP complementary peptide (Ser-Ser-Trp-Ala-Val-Leu-Glu-Val-Ala) (PVA). Rabbit anti-PVA antibodies were nonimmunoreactive with any protein in rat liver membranes or in a partially purified preparation from rat liver containing reconstitutable vasopressin binding activity. Furthermore, there was no suppression of the AVP pressor effect by PVA in vivo using a rat blood pressure bioassay. These findings do not support the hypothesis that the V1 receptor binding site is encoded by the antisense DNA strand to AVP.en
dc.language.isoenen
dc.subject.otherAmino Acid Sequenceen
dc.subject.otherAnimalsen
dc.subject.otherCell Membrane.metabolismen
dc.subject.otherImmunoblottingen
dc.subject.otherLiver.metabolismen
dc.subject.otherMolecular Sequence Dataen
dc.subject.otherOligopeptides.metabolismen
dc.subject.otherRatsen
dc.subject.otherReceptors, Angiotensin.isolation & purification.metabolismen
dc.subject.otherReceptors, Vasopressinen
dc.subject.otherVasopressinsen
dc.titleVasopressin antisense peptide interactions with the V1 receptor.en
dc.typeJournal Articleen
dc.identifier.journaltitlePeptidesen
dc.identifier.affiliationUniversity of Melbourne, Department of Medicine, Austin Hospital, Heidelberg, Victoria, Australiaen
dc.description.pages857-62en
dc.relation.urlhttps://pubmed.ncbi.nlm.nih.gov/2146598en
dc.type.austinJournal Articleen
item.openairetypeJournal Article-
item.openairecristypehttp://purl.org/coar/resource_type/c_18cf-
item.grantfulltextnone-
item.fulltextNo Fulltext-
item.cerifentitytypePublications-
item.languageiso639-1en-
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